6RTH

Crystal structure of the ligand-free glycosyltransferase domain from the YGT toxin

Summary for 6RTH

• Entry DOI: 10.2210/pdb6rth/pdb
• Descriptor: RTX toxin and Ca2+-binding protein (1 entity in total)
• Functional Keywords: glycosyltransferase domain, toxin
• Biological source: Yersinia mollaretii (strain ATCC 43969 / DSM 18520 / CIP 103324 / CNY 7263 / WAIP 204)
• Total number of polymer chains: 2
• Total formula weight: 119307.55

Authors

Wirth, C.,Bogdanovic, X.,Kao, W.-C.,Hunte, C. (deposition date: 2019-05-23, release date: 2020-03-18, Last modification date: 2024-01-24)

Primary citation

Ost, G.S.,Wirth, C.,Bogdanovic, X.,Kao, W.C.,Schorch, B.,Aktories, P.J.K.,Papatheodorou, P.,Schwan, C.,Schlosser, A.,Jank, T.,Hunte, C.,Aktories, K.
Inverse control of Rab proteins byYersiniaADP-ribosyltransferase and glycosyltransferase related to clostridial glucosylating toxins.
Sci Adv, 6:eaaz2094-eaaz2094, 2020

PubMed Abstract: We identified a glucosyltransferase (YGT) and an ADP-ribosyltransferase (YART) in , highly related to glucosylating toxins from , the cause of antibiotics-associated enterocolitis. Both toxins consist of an amino-terminal enzyme domain, an autoprotease domain activated by inositol hexakisphosphate, and a carboxyl-terminal translocation domain. YGT -acetylglucosaminylates Rab5 and Rab31 at Thr and Thr, respectively, thereby inactivating the Rab proteins. YART ADP-ribosylates Rab5 and Rab31 at Gln and Gln, respectively. This activates Rab proteins by inhibiting GTP hydrolysis. We determined the crystal structure of the glycosyltransferase domain of YGT (YGT) in the presence and absence of UDP at 1.9- and 3.4-Å resolution, respectively. Thereby, we identified a previously unknown potassium ion-binding site, which explains potassium ion-dependent enhanced glycosyltransferase activity in clostridial and related toxins. Our findings exhibit a novel type of inverse regulation of Rab proteins by toxins and provide new insights into the structure-function relationship of glycosyltransferase toxins.

PubMed: 32195351
DOI: 10.1126/sciadv.aaz2094

Experimental method

X-RAY DIFFRACTION (3.4 Å)